Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.

Trp B Protein, E. coli, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 40-50 KDa and the accession number is P0A879.

E. coli

E. coli

Tryptophan synthase β chain,Tryptophan synthase beta chain,trpB

Thr2-Ile397

Thr2-Ile397

Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.

Tryptophan synthase is an enzyme that catalyzes the final two steps in the biosynthesis of tryptophan. It is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae, but is absent from animals such as humans. Tryptophan synthase typically exists as an α-ββ-α complex.The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate: L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O.The beta subunits catalyze the irreversible condensation of indole and serine to form tryptophan in a pyridoxal phosphate (PLP) dependent reaction. Their assembly into a complex leads to structural changes in both subunits resulting in reciprocal activation.